Synaptotagmin 1 is a member of the Ca2+-binding synaptotagmin family of proteins that includes 16 members in vertebrates and is involved in regulated exocytosis and trafficking1,2.
Synaptotagmins are type I membrane proteins located in intracellular vesicles and consist of a short N-terminal domain located in the vesicle lumen, a transmembrane domain and a cytosolic domain containing two Ca2+ binding domains1,2.
Synaptotagmins are usually localized to distinct secretory vesicles and control their Ca2+-dependent fusion. Synaptotagmin I is predominantly expressed in neuronal cells and is an abundant constituent of synaptic vesicles1,2.
Synaptotagmin I has a relatively low Ca2+ affinity and is able to bind Ca2+ mostly in the vicinity of Ca2+ channels pores. Indeed, Synaptotagmin I has been demonstrated to directly interact with selected Ca2+ channels. Synaptotagmin I also binds to the t-SNARE protein Syntaxin 1 in a Ca2+-dependent manner thus forming the prototypical Ca2+-dependent fast synaptic vesicle exocytosis protein complex that also includes SNAP-25 and VAMP1,2,3.
Alomone Labs is pleased to offer a highly specific antibody directed against the intravesicular N-terminus domain of rat synaptotagmin I. Anti-Synaptotagmin I antibody (#AG1194) can be used in Western blot and immunohistochemical applications, and was designed to recognize Synaptotagmin I from rat, mouse and human samples.
